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Volume 18, Issue 2, Pages 347-353

Sequence analysis of earthworm hemolysins

Simone König,1,5 Frank Wagner,2 Ellen Kauschke,3 and Ines Eue4

1Integrated Functional Genomics, IZKF University of Münster, Germany
2Zoological Institute, University of Greifswald, Germany
3Institute of Anatomy, University of Greifswald, Germany
4In den Wolfseichen 5, Lohmar, Germany
5Integrated Functional Genomics, Von-Esmarch-Str. 56, 48149 Muenster, Germany

Copyright © 2004 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Annelids are capable of defending themselves from pathogens and of recognizing degenerated self tissue. These reactions require specialized immune mechanisms that are effected by proteins and cellular reactions. Hemolytic proteins are the most striking humoral defense molecules in the earthworm Eisenia fetida. Beside their hemolytic activity these proteins possess agglutinating, antibacterial, cytotoxic, and clotting properties. Hemolytic proteins both from coelomocytes (CL39,41) and coelomic fluid (H1−3) of wildtype E. fetida were isolated and assigned to fetidin and lysenin using mass spectrometry and bioinformatic tools. Glycosylation was found for H1. In silico analyses of the hemolysins revealed two hemolysin isoforms and consensus sites for N-glycosylation and peroxidases proximal heme-binding ligand.